The Transfer of Heavy Chains from Bikunin Proteins to Hyaluronan Requires Both TSG-6 and HC2

Sanggaard, Kristian W.; Sonne-Schmidt, Carsten S.; Krogager, Toke P.; Lorentzen, Karen A.; Wisniewski, Hans‐Georg; Thøgersen, Ida B.; Enghild, Jan J.

doi:10.1074/jbc.m800874200

Cited by 34 publications

(52 citation statements)

References 33 publications

(45 reference statements)

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“…Free bikunin containing the CS chain was purified from NaOH dissociated I␣I as described before (28). HA oligosaccharides of distinct sizes were purified from a limited chondroitinase ABC digest of polymers of HA, as described recently (16). Human TSG-6 was expressed and purified, also as described before (23,29).…”

Section: Methodsmentioning

confidence: 99%

“…The incubation with oligo-HA (samples iii and iv) was done for 2 h at 37°C in TBS containing 1 mM MgCl 2 and with the addition of 1 g of TSG-6. the HC transfer, free bikunin is produced (15,16), but it is unclear whether the generated stripped bikunin is able to act as HC acceptor. This was investigated by fluorescently labeling purified free bikunin (we use the term free bikunin for CSsubstituted bikunin, which is not in complex with HCs) and incubating with TSG-6 and different bikunin proteins.…”

Section: Comparison Of the Authentic Hc Position On The Cs And The Hcmentioning

confidence: 99%

“…In the second transesterification, the transient ester bond is cleaved and reformed between the C terminus of the HCs and HA (14). HC2 is required during both transesterification reactions, but the molecular mechanism is currently unknown (16). In addition to HA, C-0-S and the CS chain of the bikunin proteins may also function as HC acceptors during this reaction (15,16,18).…”

mentioning

confidence: 99%

“…HC2 is required during both transesterification reactions, but the molecular mechanism is currently unknown (16). In addition to HA, C-0-S and the CS chain of the bikunin proteins may also function as HC acceptors during this reaction (15,16,18). The attachment of HCs to the bikunin CS chain generates new proteins designated HMW bikunin proteins (15,16).…”

mentioning

confidence: 99%

“…In addition to HA, C-0-S and the CS chain of the bikunin proteins may also function as HC acceptors during this reaction (15,16,18). The attachment of HCs to the bikunin CS chain generates new proteins designated HMW bikunin proteins (15,16). The physiological importance of TSG-6 and of the unique interactions between TSG-6, bikunin proteins, and HA have been underlined in many different studies (19 -24), particularly the importance during the formation of the HA-rich extracellular matrix surrounding the oocyte in mammals (25)(26)(27).…”

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confidence: 99%

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The TSG-6/HC2-mediated Transfer Is a Dynamic Process Shuffling Heavy Chains between Glycosaminoglycans

Sanggaard

Scavenius

Rasmussen

et al. 2010

Journal of Biological Chemistry

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The heavy chain (HC) subunits of the bikunin proteins are covalently attached to a single chondroitin sulfate (CS) chain originating from bikunin and can be transferred to different hyaluronan (HA) molecules by TSG-6/HC2. In the present study, we demonstrate that HCs transferred to HA may function as HC donors in subsequent transfer reactions, and we show that the CS of bikunin may serve as an HC acceptor, analogous to HA. Our data suggest that TSG-6/HC2 link HCs randomly on the CS chain of bikunin, in contrast to the ordered attachment observed during the biosynthesis. Moreover, the results show that the transfer activity is indifferent to the new HC position, and the relocated HCs are thus prone to further TSG-6/HC2-induced transfer reactions. The data suggest that HCs may be transferred directly from HA to HA without the involvement of the bikunin CS chain. The results demonstrate reversibility of the interactions between HCs and glycosaminoglycans and suggest that a dynamic shuffling of the HCs occur in vivo.

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Section: Methodsmentioning

confidence: 99%

Section: Comparison Of the Authentic Hc Position On The Cs And The Hcmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The TSG-6/HC2-mediated Transfer Is a Dynamic Process Shuffling Heavy Chains between Glycosaminoglycans

Sanggaard

Scavenius

Rasmussen

et al. 2010

Journal of Biological Chemistry

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Urine inter‐alpha‐trypsin inhibitor family‐related proteins may serve as biomarkers for disease activity of lupus

Jiang

Zhao

Wang

et al. 2022

Clinical Laboratory Analysis

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Background Systemic lupus erythematosus (SLE) is a chronic inflammatory disease involving multiple tissues. Inter‐Alpha‐Trypsin Inhibitor (ITI) family proteins have a role in maintaining tissue homeostasis, but their possible clinical significance in the SLE patients has not been reported. The aim of this study was to analyze and verify the expression of ITI‐related proteins in the urine of SLE patients, further explore the features of these proteins in disease activity. Methods Based on label‐free proteomics technology and bioinformatics technology, we analyzed the expression of ITI family‐related proteins in the urine of lupus. Subsequently, Western‐blot and targeted proteomics were used to qualitatively and quantitatively verify the expression of these proteins, respectively. Results A total of seven ITI family‐related proteins were screened and identified; and six of these proteins were differentially expressed in the urine of SLE patients. Further quantitative analysis showed that the expressions of ITIH2, ECM1, and ITIH5 in urine between active SLE group and stable SLE group were consistent with the preliminary screening results. The expression of ITIH2 and ECM1 in the renal damage group were also consistent with the screening results. Moreover, ITIH2 and ECM1 have a good correlation with disease activity and have a certain correlation with renal damage. Conclusions In this exploratory study, we evaluated the expression of ITI family‐related proteins in the urine of SLE and found that urine ITIH2 and ECM1 were closely related to SLE activity, especially kidney damage, providing an experimental basis for further exploration of the potential roles in monitoring lupus and lupus nephritis activity.

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Inter-α-inhibitor Proteins: A Review of Structure and Function

Garantziotis

2023

Biology of Extracellular Matrix

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The Transfer of Heavy Chains from Bikunin Proteins to Hyaluronan Requires Both TSG-6 and HC2

Cited by 34 publications

References 33 publications

The TSG-6/HC2-mediated Transfer Is a Dynamic Process Shuffling Heavy Chains between Glycosaminoglycans

The TSG-6/HC2-mediated Transfer Is a Dynamic Process Shuffling Heavy Chains between Glycosaminoglycans

Urine inter‐alpha‐trypsin inhibitor family‐related proteins may serve as biomarkers for disease activity of lupus

Inter-α-inhibitor Proteins: A Review of Structure and Function

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